{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,17]],"date-time":"2026-09-17T19:54:23Z","timestamp":1789674863762,"version":"4.0.1"},"reference-count":49,"publisher":"MDPI AG","issue":"14","license":[{"start":{"date-parts":[[2025,7,20]],"date-time":"2025-07-20T00:00:00Z","timestamp":1752969600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"name":"Excellence Initiative\u2014Debuts, under the \u201cExcellence Initiative\u2014Research University\u201d program, NCU in Toru\u0144","award":["9\/2022\/Debiuty3"],"award-info":[{"award-number":["9\/2022\/Debiuty3"]}]},{"name":"Excellence Initiative\u2014Debuts, under the \u201cExcellence Initiative\u2014Research University\u201d program, NCU in Toru\u0144","award":["6\/2022\/Debiuty3"],"award-info":[{"award-number":["6\/2022\/Debiuty3"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>The growing need for developing safer and more effective methods for obtaining enantiomers of chiral compounds, particularly those with pharmacological activity, highlights the potential of biocatalysis as an appropriate pharmaceutical research direction. However, low catalytic activity and stability of free enzymes are often among the substantial limitations to the wide application of biocatalysis. Therefore, to overcome these obstacles, new technological procedures are being designed. In this study, we present optimized protocols for the immobilization of Candida antarctica lipase B (CALB) on an octyl- agarose support, ensuring high enantioselectivity in an organic reaction medium. The immobilization procedures (with drying step), including buffers with different pH values and concentrations, as well as the study of the influence of temperature and immobilization time, were presented. It was found that the optimal conditions were provided by citrate buffer with a pH of 4 and a concentration of 300 mM. The immobilized CALB on the octyl-agarose support exhibited high catalytic activity in the kinetic resolution of (R,S)-1-phenylethanol via enantioselective transesterification with isopropenyl acetate in 1,2-dichloropropane (DCP), as a model reaction for lipase activity monitoring on an analytical scale. HPLC analysis demonstrated that the (R)-1-phenylethyl acetate was obtained in an enantiomeric excess of eep &gt; 99% at a conversion of approximately 40%, and the enantiomeric ratio was E &gt; 200. Thermal and storage stability studies performed on the immobilized CALB octyl-agarose support confirmed its excellent stability. After 7 days of thermal stability testing at 65 \u00b0C in a climatic chamber, the (R)-1-phenylethyl acetate was characterized by enantiomeric excess of eep &gt; 99% at a conversion of around 40% (similar values of catalytic parameters to those achieved using a non-stored lipase). The documented high catalytic activity and stability of the developed CALB-octyl-agarose support allow us to consider it as a useful tool for enantioselective transesterification in organic medium.<\/jats:p>","DOI":"10.3390\/ijms26146961","type":"journal-article","created":{"date-parts":[[2025,7,21]],"date-time":"2025-07-21T09:33:53Z","timestamp":1753090433000},"page":"6961","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":4,"title":["CALB Immobilized on Octyl-Agarose\u2014An Efficient Pharmaceutical Biocatalyst for Transesterification in Organic Medium"],"prefix":"10.3390","volume":"26","author":[{"given":"Joanna","family":"Si\u00f3dmiak","sequence":"first","affiliation":[{"name":"Department of Laboratory Medicine, Faculty of Pharmacy, Ludwik Rydygier Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toru\u0144, 85-094 Bydgoszcz, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Jacek","family":"Dul\u0119ba","sequence":"additional","affiliation":[{"name":"Department of Pharmacy Practice, Faculty of Pharmacy, Ludwik Rydygier Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toru\u0144, 85-089 Bydgoszcz, Poland"},{"name":"Department of Pharmaceutical Technology, Faculty of Pharmacy, Medical Biotechnology and Laboratory Medicine, Pomeranian Medical University in Szczecin, 71-251 Szczecin, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-9107-263X","authenticated-orcid":false,"given":"Natalia","family":"Kocot","sequence":"additional","affiliation":[{"name":"Doctoral School of Medical and Health Sciences, Jagiellonian University, 31-530 Krak\u00f3w, Poland"},{"name":"Department of Pharmaceutical Biochemistry, Faculty of Pharmacy, Jagiellonian University Medical College, 30-688 Krak\u00f3w, Poland"},{"name":"Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toru\u0144, 85-089 Bydgoszcz, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-8111-8945","authenticated-orcid":false,"given":"Rafa\u0142","family":"Mastalerz","sequence":"additional","affiliation":[{"name":"Department of Medicinal Chemistry, Faculty of Pharmacy, Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toru\u0144, 85-089 Bydgoszcz, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-5664-2745","authenticated-orcid":false,"given":"Gudmundur G.","family":"Haraldsson","sequence":"additional","affiliation":[{"name":"Science Institute, University of Iceland, 107 Reykjavik, Iceland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-9232-5798","authenticated-orcid":false,"given":"Tomasz","family":"Si\u00f3dmiak","sequence":"additional","affiliation":[{"name":"Department of Pharmacy Practice, Faculty of Pharmacy, Ludwik Rydygier Collegium Medicum in Bydgoszcz, Nicolaus Copernicus University in Toru\u0144, 85-089 Bydgoszcz, Poland"},{"name":"Department of Pharmaceutical Technology, Faculty of Pharmacy, Medical Biotechnology and Laboratory Medicine, Pomeranian Medical University in Szczecin, 71-251 Szczecin, Poland"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"1968","published-online":{"date-parts":[[2025,7,20]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","first-page":"e23698","DOI":"10.1002\/chir.23698","article-title":"Expanding the Role of Chiral Drugs and Chiral Nanomaterials as a Potential Therapeutic Tool","volume":"36","author":"Satapathy","year":"2024","journal-title":"Chirality"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"3133","DOI":"10.1021\/acs.cgd.3c01030","article-title":"Chiral Inversion of Thalidomide During Crystal Growth by Sublimation","volume":"24","author":"Kira","year":"2024","journal-title":"Cryst. Growth Des."},{"key":"ref_3","doi-asserted-by":"crossref","unstructured":"Cizm\u00e1rikov\u00e1, R., Cizm\u00e1rik, J., Valentov\u00e1, J., Habala, L., and Markuliak, M. (2020). Chiral Aspects of Local Anesthetics. Molecules, 25.","DOI":"10.3390\/molecules25122738"},{"key":"ref_4","doi-asserted-by":"crossref","first-page":"33429","DOI":"10.1039\/D4RA05694A","article-title":"The significance of chirality in contemporary drug discovery-a mini review","volume":"14","author":"Senkuttuvan","year":"2024","journal-title":"RSC Adv."},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"e202405153","DOI":"10.1002\/slct.202405153","article-title":"Green Synthesis of Repotrectinib: Impact of Aqueous Micellar Media on Chemoenzymatic Transformations","volume":"9","author":"Rajendra","year":"2024","journal-title":"ChemistrySelect"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Scheibel, D., Gitsov, I., and Gitsov, I. (2024). Enzymes in \u201cGreen\u201d Synthetic Chemistry: Laccase and Lipase. Molecules, 29.","DOI":"10.3390\/molecules29050989"},{"key":"ref_7","doi-asserted-by":"crossref","first-page":"3854","DOI":"10.1021\/acs.jcim.3c00194","article-title":"The Conformational Transitions and Dynamics of Burkholderia cepacia Lipase Regulated by Water-Oil Interfaces","volume":"63","author":"Liang","year":"2023","journal-title":"J. Chem. Inf. Model."},{"key":"ref_8","first-page":"18262","article-title":"Hydrophobic Residues Promote Interfacial Activation of Candida rugosa Lipase: A Study of Rotational Dynamics","volume":"40","author":"Waggett","year":"2024","journal-title":"Langmuir"},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1007\/s00706-023-03147-3","article-title":"Fatty and aromatic acids as acyl donors in enzymatic kinetic resolution of phenylethanol and 1-phenylpropan-2-ol","volume":"155","author":"Smaine","year":"2024","journal-title":"Monatsh. Chem."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"1052","DOI":"10.1021\/acs.chemrev.1c00574","article-title":"Shortening Synthetic Routes to Small Molecule Active Pharmaceutical Ingredients Employing Biocatalytic Methods","volume":"122","author":"Schmermund","year":"2022","journal-title":"Chem. Rev."},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Gundersen, M., Austli, G., Lovland, S., Hansen, M., Rodseth, M., and Jacobsen, E. (2021). Lipase Catalyzed Synthesis of Enantiopure Precursors and Derivatives for \u03b2-Blockers Practolol, Pindolol and Carteolol. Catalysts, 11.","DOI":"10.3390\/catal11040503"},{"key":"ref_12","first-page":"50","article-title":"Insight into microwave assisted enzyme catalysis in process intensification of reaction and selectivity: Kinetic resolution of (R,S)-flurbiprofen with alcohols","volume":"440","author":"Gupta","year":"2017","journal-title":"Mol. Catal."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"15733","DOI":"10.1021\/acs.iecr.3c02132","article-title":"Application of Lipase B from Candida antarctica in the Pharmaceutical Industry","volume":"62","author":"Wang","year":"2023","journal-title":"Ind. Eng. Chem. Res."},{"key":"ref_14","first-page":"111529","article-title":"Synthesis of lipase\/silica biocatalysts through the immobilization of CALB on porous SBA-15 and their application on the resolution of pharmaceutical derivatives and on nutraceutical enrichment of natural oil","volume":"505","author":"Cipolatti","year":"2021","journal-title":"Mol. Catal."},{"key":"ref_15","doi-asserted-by":"crossref","first-page":"186","DOI":"10.1016\/j.foodchem.2018.10.111","article-title":"Lipase-catalyzed synthesis mechanism of tri-acetylated phloridzin and its antiproliferative activity against HepG2 cancer cells","volume":"277","author":"Chen","year":"2019","journal-title":"Food Chem."},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"1782","DOI":"10.1002\/cctc.201902292","article-title":"Dual Mechanoenzymatic Kinetic Resolution of (\u00b1)-Ketorolac","volume":"12","author":"Juaristi","year":"2020","journal-title":"ChemCatChem"},{"key":"ref_17","doi-asserted-by":"crossref","unstructured":"Zappaterra, F., Costa, S., Summa, D., Semeraro, B., Cristofori, V., Trapella, C., and Tamburini, E. (2021). Glyceric Prodrug of Ursodeoxycholic Acid (UDCA): Novozym 435-Catalyzed Synthesis of UDCA-Monoglyceride. Molecules, 26.","DOI":"10.3390\/molecules26195966"},{"key":"ref_18","doi-asserted-by":"crossref","unstructured":"Xiang, Z., Chen, Y., Ma, K., Ye, Y., Zheng, L., Yang, Y., Li, Y., and Jin, X. (2013). The role of Ursodeoxycholic acid in non-alcoholic steatohepatitis: A systematic review. BMC Gastroenterol, 13.","DOI":"10.1186\/1471-230X-13-140"},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"798","DOI":"10.2174\/1385272824666200408092305","article-title":"Amano Lipase PS from Burkholderia cepacia\u2014Evaluation of the Effect of Substrates and Reaction Media on the Catalytic Activity","volume":"24","year":"2020","journal-title":"Curr. Org. Chem."},{"key":"ref_20","doi-asserted-by":"crossref","first-page":"126","DOI":"10.1016\/j.procbio.2022.06.003","article-title":"The influence of substrate systems on the enantioselective and lipolytic activity of immobilized Amano PS from Burkholderia cepacia lipase (APS-BCL)","volume":"120","year":"2022","journal-title":"Process Biochem."},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"2822","DOI":"10.1021\/jacs.4c16145","article-title":"Upcycling Poly(vinyl chloride) and Polystyrene Plastics Using Photothermal Conversion","volume":"147","author":"Jiang","year":"2025","journal-title":"J. Am. Chem. Soc."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"131041","DOI":"10.1016\/j.seppur.2024.131041","article-title":"Enzyme synthesis and continuous flow separation of (R)-1-phenylethanol in a modular microfluidic system","volume":"360","author":"Sauer","year":"2025","journal-title":"Sep. Purif. Technol."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"Ferraccioli, R. (2021). Progress on the Stereoselective Synthesis of Chiral Molecules Based on Metal-Catalyzed Dynamic Kinetic Resolution of Alcohols with Lipases. Symmetry-Basel, 13.","DOI":"10.3390\/sym13091744"},{"key":"ref_24","doi-asserted-by":"crossref","unstructured":"Stradomska, D., Heba, M., Czernek, A., Ku\u017anik, N., Gillner, D., Maresz, K., Pud\u0142o, W., Jarz\u0119bski, A., and Szyma\u0144ska, K. (2021). Lipase Immobilized on MCFs as Biocatalysts for Kinetic and Dynamic Kinetic Resolution of sec-Alcohols. Catalysts, 11.","DOI":"10.3390\/catal11040518"},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"152424","DOI":"10.1016\/j.tetlet.2020.152424","article-title":"CO2-expanded liquids as solvents to enhance activity of Pseudozyma antarctica lipase B towards ortho-substituted 1-phenylethanols","volume":"61","author":"Otsu","year":"2020","journal-title":"Tetrahedron Lett."},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"110517","DOI":"10.1016\/j.enzmictec.2024.110517","article-title":"Changes in ficin specificity by different substrate proteins promoted by enzyme immobilization","volume":"181","author":"Hocine","year":"2024","journal-title":"Enzyme Microb. Technol."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"120014","DOI":"10.1016\/j.indcrop.2024.120014","article-title":"Improving the performance of lipases in the full hydrolysis of residual coconut oil by immobilization on hydrophobic supports","volume":"222","author":"Monteiro","year":"2024","journal-title":"Ind. Crops Prod."},{"key":"ref_28","doi-asserted-by":"crossref","unstructured":"Guimaraes, J., Carballares, D., Rocha-Martin, J., Alc\u00e1ntara, A., Tardioli, P., and Fernandez-Lafuente, R. (2023). Heterofunctional Methacrylate Beads Bearing Octadecyl and Vinyl Sulfone Groups: Tricks to Obtain an Interfacially Activated Lipase from Thermomyces lanuginosus and Covalently Attached to the Support. Catalysts, 13.","DOI":"10.3390\/catal13010108"},{"key":"ref_29","doi-asserted-by":"crossref","unstructured":"Rueda, N., Albuquerque, T., Bartolome-Cabrero, R., Fernandez-Lopez, L., Torres, R., Ortiz, C., dos Santos, J., Barbosa, O., and Fernandez-Lafuente, R. (2016). Reversible Immobilization of Lipases on Heterofunctional Octyl-Amino Agarose Beads Prevents Enzyme Desorption. Molecules, 21.","DOI":"10.3390\/molecules21050646"},{"key":"ref_30","doi-asserted-by":"crossref","unstructured":"Si\u00f3dmiak, T., Dul\u0119ba, J., Haraldsson, G.G., Si\u00f3dmiak, J., and Marsza\u0142\u0142, M.P. (2023). The Studies of Sepharose-Immobilized Lipases: Combining Techniques for the Enhancement of Activity and Thermal Stability. Catalysts, 13.","DOI":"10.3390\/catal13050887"},{"key":"ref_31","doi-asserted-by":"crossref","unstructured":"Si\u00f3dmiak, T., Si\u00f3dmiak, J., Mastalerz, R., Kocot, N., Dul\u0119ba, J., Haraldsson, G.G., W\u0105tr\u00f3bska-\u015awietlikowska, D., and Marsza\u0142\u0142, M.P. (2023). Climatic Chamber Stability Tests of Lipase-Catalytic Octyl-Sepharose Systems. Catalysts, 13.","DOI":"10.3390\/catal13030501"},{"key":"ref_32","doi-asserted-by":"crossref","unstructured":"Si\u00f3dmiak, J., Dul\u0119ba, J., Kocot, N., Mastalerz, R., Haraldsson, G.G., Marsza\u0142\u0142, M.P., and Si\u00f3dmiak, T. (2024). A New Approach in Lipase-Octyl-Agarose Biocatalysis of 2-Arylpropionic Acid Derivatives. Int. J. Mol. Sci., 25.","DOI":"10.3390\/ijms25105084"},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"108","DOI":"10.1016\/j.colsurfb.2015.04.041","article-title":"Conformation and activity of lipase B from Candida antarctica in bicontinuous microemulsions","volume":"131","author":"Subinya","year":"2015","journal-title":"Colloids Surf. B Biointerfaces"},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"1700266","DOI":"10.1002\/ejlt.201700266","article-title":"Immobilization of Candida antarctica Lipase B Onto ECR1030 Resin and its Application in the Synthesis of n-3 PUFA-Rich Triacylglycerols","volume":"119","author":"Li","year":"2017","journal-title":"Eur. J. Lipid Sci. Technol."},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"20","DOI":"10.1016\/j.procbio.2023.08.003","article-title":"The nature of the buffer alters the effects of the chemical modification on the stability of immobilized lipases","volume":"133","author":"Carballares","year":"2023","journal-title":"Process Biochem."},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Abellanas-Perez, P., Carballares, D., Rocha-Martin, J., and Fernandez-Lafuente, R. (2024). The Effects of Buffer Nature on Immobilized Lipase Stability Depend on Enzyme Support Loading. Catalysts, 14.","DOI":"10.3390\/catal14020105"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"11499","DOI":"10.1021\/acs.langmuir.1c01726","article-title":"Molecular Mechanistic Insights into the Ionic-Strength-Controlled Interfacial Behavior of Proteins on a TiO2 Surface","volume":"37","author":"Dong","year":"2021","journal-title":"Langmuir"},{"key":"ref_38","doi-asserted-by":"crossref","unstructured":"Alnoch, R.C., dos Santos, L.A., de Almeida, J.M., Krieger, N., and Mateo, C. (2020). Recent Trends in Biomaterials for Immobilization of Lipases for Application in Non-Conventional Media. Catalysts, 10.","DOI":"10.3390\/catal10060697"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"110583","DOI":"10.1016\/j.enzmictec.2025.110583","article-title":"Effect of the support alkyl chain nature in the functional properties of the immobilized lipases","volume":"184","author":"Polizeli","year":"2025","journal-title":"Enzyme Microb. Technol."},{"key":"ref_40","doi-asserted-by":"crossref","unstructured":"Abdelkader, I., Guis\u00e1n, J., Sayari, A., and Fern\u00e1ndez-Lorente, G. (2024). Various Strategies for the Immobilization of a Phospholipase C from Bacillus cereus for the Modulation of Its Biochemical Properties. Molecules, 29.","DOI":"10.3390\/molecules29071467"},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"3152","DOI":"10.1007\/s12010-024-05175-z","article-title":"Optimizing Thermal Stability: Evaluating the Impact of Heterofunctional Hydrophobic Supports on Immobilized Flaxseed Lipase","volume":"197","author":"Tardioli","year":"2025","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_42","doi-asserted-by":"crossref","unstructured":"Sabi, G., de Souza, L., Abellanas-Perez, P., Tardioli, P., Mendes, A., Rocha-Martin, J., and Fernandez-Lafuente, R. (2025). Enzyme loading in the support and medium composition during immobilization alter activity, specificity and stability of octyl agarose-immobilized Eversa Transform. Int. J. Biol. Macromol., 295.","DOI":"10.1016\/j.ijbiomac.2025.139667"},{"key":"ref_43","doi-asserted-by":"crossref","unstructured":"Abellanas-Perez, P., de Andrades, D., Alcantara, A., Rocha-Martin, J., Polizeli, M., and Fernandez-Lafuente, R. (2025). Vinyl sulfone-amino-alkyl supports: Heterofunctional matrixes to prevent enzyme release and stabilize lipases via covalent immobilization. Int. J. Biol. Macromol., 310.","DOI":"10.1016\/j.ijbiomac.2025.143305"},{"key":"ref_44","doi-asserted-by":"crossref","first-page":"130","DOI":"10.1016\/j.cattod.2020.03.059","article-title":"Immobilization of lipases via interfacial activation on hydrophobic supports: Production of biocatalysts libraries by altering the immobilization conditions","volume":"362","author":"Rios","year":"2021","journal-title":"Catalysis Today"},{"key":"ref_45","doi-asserted-by":"crossref","unstructured":"Arana-Pena, S., Carballares, D., Corberan, V.C., and Fernandez-Lafuente, R. (2020). Multi-Combilipases: Co-Immobilizing Lipases with Very Different Stabilities Combining Immobilization via Interfacial Activation and Ion Exchange. The Reuse of the Most Stable Co-Immobilized Enzymes after Inactivation of the Least Stable Ones. Catalysts, 10.","DOI":"10.3390\/catal10101207"},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"839","DOI":"10.1002\/aocs.12833","article-title":"Improving the stability of an unstable lipase by applying different immobilization strategies for the selective hydrolysis of fish oil","volume":"101","author":"Ahrari","year":"2024","journal-title":"J. Am. Oil Chem. Soc."},{"key":"ref_47","doi-asserted-by":"crossref","unstructured":"Si\u00f3dmiak, T., Haraldsson, G.G., Dul\u0119ba, J., Ziegler-Borowska, M., Si\u00f3dmiak, J., and Marsza\u0142\u0142, M.P. (2020). Evaluation of Designed Immobilized Catalytic Systems: Activity Enhancement of Lipase B from Candida antarctica. Catalysts, 10.","DOI":"10.3390\/catal10080876"},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"2769","DOI":"10.1007\/s12010-014-1455-4","article-title":"High Enantioselective Novozym 435-Catalyzed Esterification of (R,S)-Flurbiprofen Monitored with a Chiral Stationary Phase","volume":"175","author":"Mangelings","year":"2015","journal-title":"Appl. Biochem. Biotechnol."},{"key":"ref_49","doi-asserted-by":"crossref","unstructured":"Cha\u0142upka, J., Dul\u0119ba, J., Sikora, A., Si\u00f3dmiak, T., and Marsza\u0142\u0142, M.P. (2023). The Application of Two-Phase Catalytic System in Enantioselective Separation of Racemic (R,S)-1-Phenylethanol. Catalysts, 13.","DOI":"10.3390\/catal13020292"}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/14\/6961\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,10,9]],"date-time":"2025-10-09T18:12:51Z","timestamp":1760033571000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/14\/6961"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,7,20]]},"references-count":49,"journal-issue":{"issue":"14","published-online":{"date-parts":[[2025,7]]}},"alternative-id":["ijms26146961"],"URL":"https:\/\/doi.org\/10.3390\/ijms26146961","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,7,20]]}}}